메뉴 건너뛰기




Volumn 25, Issue 24, 2005, Pages 10822-10832

Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; MATRIX PROTEIN; PEROXIN; PROTEIN PEX14; PROTEIN PEX2; PROTEIN PEX26; PROTEIN PEX5; PROTEIN PEX5L; PROTEIN PEX7; PROTEIN PTS2; SULFUR 35; UNCLASSIFIED DRUG;

EID: 28544451220     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.24.10822-10832.2005     Document Type: Article
Times cited : (179)

References (58)
  • 2
    • 0030890954 scopus 로고    scopus 로고
    • Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways
    • Albertini, M., P. Rehling, R. Erdmann, W. Girzalsky, J. A. K. W. Kiel, M. Veenhuis, and W.-H. Kunau. 1997. Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways. Cell 89:83-92.
    • (1997) Cell , vol.89 , pp. 83-92
    • Albertini, M.1    Rehling, P.2    Erdmann, R.3    Girzalsky, W.4    Kiel, J.A.K.W.5    Veenhuis, M.6    Kunau, W.-H.7
  • 3
    • 0033739464 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae PTS1 receptor Pex5p interacts with the SH3 domain of the peroxisomal membrane protein Pex13p in an unconventional, non-PXXP-related manner
    • Bottger, G., P. Barnett, A. T. J. Klein, A. Kragt, H. F. Tabak, and B. Distel. 2000. Saccharomyces cerevisiae PTS1 receptor Pex5p interacts with the SH3 domain of the peroxisomal membrane protein Pex13p in an unconventional, non-PXXP-related manner. Mol. Biol. Cell 11:3963-3976.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3963-3976
    • Bottger, G.1    Barnett, P.2    Klein, A.T.J.3    Kragt, A.4    Tabak, H.F.5    Distel, B.6
  • 4
    • 0033571690 scopus 로고    scopus 로고
    • PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein import
    • Chang, C.-C., D. S. Warren, K. A. Sacksteder, and S. J. Gould. 1999. PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein import. J. Cell Biol. 147:761-774.
    • (1999) J. Cell Biol. , vol.147 , pp. 761-774
    • Chang, C.-C.1    Warren, D.S.2    Sacksteder, K.A.3    Gould, S.J.4
  • 5
    • 0033800536 scopus 로고    scopus 로고
    • The peroxisome biogenesis factors Pex4p, Pex22p, Pex1p, and Pex6p act in the terminal steps of peroxisomal matrix protein import
    • Collins, C. S., J. E. Kalish, J. C. Morrell, J. M. McCaffery, and S. J. Gould. 2000. The peroxisome biogenesis factors Pex4p, Pex22p, Pex1p, and Pex6p act in the terminal steps of peroxisomal matrix protein import. Mol. Cell. Biol. 20:7516-7526.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7516-7526
    • Collins, C.S.1    Kalish, J.E.2    Morrell, J.C.3    McCaffery, J.M.4    Gould, S.J.5
  • 6
    • 0035917528 scopus 로고    scopus 로고
    • The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol
    • Dammai, V., and S. Subramani. 2001. The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol. Cell 105:187-196.
    • (2001) Cell , vol.105 , pp. 187-196
    • Dammai, V.1    Subramani, S.2
  • 7
    • 0030845840 scopus 로고    scopus 로고
    • The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44
    • Dekker, P. J., F. Martin, A. C. Maarse, U. Bomer, H. Mueller, B. Guiard, M. Meijer, J. Rassow, and N. Pfanner. 1997. The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44. EMBO J. 16:5408-5419.
    • (1997) EMBO J. , vol.16 , pp. 5408-5419
    • Dekker, P.J.1    Martin, F.2    Maarse, A.C.3    Bomer, U.4    Mueller, H.5    Guiard, B.6    Meijer, M.7    Rassow, J.8    Pfanner, N.9
  • 8
    • 0030459304 scopus 로고    scopus 로고
    • Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: Evidence that PTS1 protein import is mediated by a cycling receptor
    • Dodt, G., and S. J. Gould. 1996. Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: evidence that PTS1 protein import is mediated by a cycling receptor. J. Cell Biol. 135:1763-1774.
    • (1996) J. Cell Biol. , vol.135 , pp. 1763-1774
    • Dodt, G.1    Gould, S.J.2
  • 9
    • 0028916868 scopus 로고
    • Identification and characterization of the putative human peroxisomal C-terminal targeting signal import receptor
    • Fransen, M., C. Brees, E. Baumgart, J. C. Vanhooren, M. Baes, G. P. Mannaerts, and P. P. V. Veldhoven. 1995. Identification and characterization of the putative human peroxisomal C-terminal targeting signal import receptor. J. Biol. Chem. 270:7731-7736.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7731-7736
    • Fransen, M.1    Brees, C.2    Baumgart, E.3    Vanhooren, J.C.4    Baes, M.5    Mannaerts, G.P.6    Veldhoven, P.P.V.7
  • 10
    • 0032493298 scopus 로고    scopus 로고
    • Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import
    • Fransen, M., S. R. Terlecky, and S. Subramani. 1998. Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import. Proc. Natl. Acad. Sci. USA 95:8087-8092.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8087-8092
    • Fransen, M.1    Terlecky, S.R.2    Subramani, S.3
  • 11
    • 0034733909 scopus 로고    scopus 로고
    • Peroxisome biogenesis and peroxisome biogenesis disorders
    • Fujiki, Y. 2000. Peroxisome biogenesis and peroxisome biogenesis disorders. FEBS Lett. 476:42-46.
    • (2000) FEBS Lett. , vol.476 , pp. 42-46
    • Fujiki, Y.1
  • 13
    • 0033134119 scopus 로고    scopus 로고
    • Newly identified Chinese hamster ovary cell mutants defective in peroxisome assembly represent complementation group a of human peroxisome biogenesis disorders and one novel group in mammals
    • Ghaedi, K., A. Itagaki, R. Toyama, S. Tamura, T. Matsumura, A. Kawai, N. Shimozawa, Y. Suzuki, N. Kondo, and Y. Fujiki. 1999. Newly identified Chinese hamster ovary cell mutants defective in peroxisome assembly represent complementation group A of human peroxisome biogenesis disorders and one novel group in mammals. Exp. Cell Res. 248:482-488.
    • (1999) Exp. Cell Res. , vol.248 , pp. 482-488
    • Ghaedi, K.1    Itagaki, A.2    Toyama, R.3    Tamura, S.4    Matsumura, T.5    Kawai, A.6    Shimozawa, N.7    Suzuki, Y.8    Kondo, N.9    Fujiki, Y.10
  • 14
    • 0033134180 scopus 로고    scopus 로고
    • Isolation and characterization of novel peroxisome biogenesis-defective Chinese hamster ovary cell mutants using green fluorescent protein
    • Ghaedi, K., A. Kawai, K. Okumoto, S. Tamura, N. Shimozawa, Y. Suzuki, N. Kondo, and Y. Fujiki. 1999. Isolation and characterization of novel peroxisome biogenesis-defective Chinese hamster ovary cell mutants using green fluorescent protein. Exp. Cell Res. 248:489-497.
    • (1999) Exp. Cell Res. , vol.248 , pp. 489-497
    • Ghaedi, K.1    Kawai, A.2    Okumoto, K.3    Tamura, S.4    Shimozawa, N.5    Suzuki, Y.6    Kondo, N.7    Fujiki, Y.8
  • 15
    • 0029795686 scopus 로고    scopus 로고
    • Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTS1 receptor
    • Gould, S. J., J. E. Kalish, J. C. Morrell, J. Bjorkman, A. J. Urquhart, and D. I. Crane. 1996. Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTS1 receptor. J. Cell Biol. 135:85-95.
    • (1996) J. Cell Biol. , vol.135 , pp. 85-95
    • Gould, S.J.1    Kalish, J.E.2    Morrell, J.C.3    Bjorkman, J.4    Urquhart, A.J.5    Crane, D.I.6
  • 17
    • 0037414755 scopus 로고    scopus 로고
    • Characterization of the peroxisomal cycling receptor. Pex5p, using a cell-free in vitro import system
    • Gouveia, A. M., C. P. Guimaraes, M. E. Oliveira, C. Reguenga, C. Sa-Miranda, and J. E. Azevedo. 2003. Characterization of the peroxisomal cycling receptor. Pex5p, using a cell-free in vitro import system. J. Biol. Chem. 278:226-232.
    • (2003) J. Biol. Chem. , vol.278 , pp. 226-232
    • Gouveia, A.M.1    Guimaraes, C.P.2    Oliveira, M.E.3    Reguenga, C.4    Sa-Miranda, C.5    Azevedo, J.E.6
  • 19
    • 0017762851 scopus 로고
    • Biogenesis of the mitochondrial matrix enzyme, glutamate dehydrogenase, in rat liver cells. I. Subcellular localization, biosynthesis, and intracellular translocation of glutamate dehydrogenase
    • Kawajiri, K., T. Harano, and T. Omura. 1977. Biogenesis of the mitochondrial matrix enzyme, glutamate dehydrogenase, in rat liver cells. I. Subcellular localization, biosynthesis, and intracellular translocation of glutamate dehydrogenase. J. Biochem. 82:1403-1416.
    • (1977) J. Biochem. , vol.82 , pp. 1403-1416
    • Kawajiri, K.1    Harano, T.2    Omura, T.3
  • 20
    • 0033153237 scopus 로고    scopus 로고
    • Dislocation of membrane proteins in FtsH-mediated proteolysis
    • Kihara, A., Y. Akiyama, and K. Ito. 1999. Dislocation of membrane proteins in FtsH-mediated proteolysis. EMBO J. 18:2970-2981.
    • (1999) EMBO J. , vol.18 , pp. 2970-2981
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 21
    • 15444353327 scopus 로고    scopus 로고
    • Newly identified Chinese hamster ovary cell mutants are defective in biogenesis of peroxisomal membrane vesicles (peroxisomal ghosts), representing a novel complementation group in mammals
    • Kinoshita, N., K. Ghaedi, N. Shimozawa, R. J. A. Wanders, Y. Matsuzono, T. Imanaka, K. Okumoto, Y. Suzuki, N. Kondo, and Y. Fujiki. 1998. Newly identified Chinese hamster ovary cell mutants are defective in biogenesis of peroxisomal membrane vesicles (peroxisomal ghosts), representing a novel complementation group in mammals. J. Biol. Chem. 273:24122-24130.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24122-24130
    • Kinoshita, N.1    Ghaedi, K.2    Shimozawa, N.3    Wanders, R.J.A.4    Matsuzono, Y.5    Imanaka, T.6    Okumoto, K.7    Suzuki, Y.8    Kondo, N.9    Fujiki, Y.10
  • 23
    • 0033639076 scopus 로고    scopus 로고
    • Membrane protein degradation by AAA proteases in mitochondria: Extraction of substrates from either membrane surface
    • Leonhard, K., B. Guiard, G. Pellecchia, A. Tzagoloff, W. Neupert, and T. Langer. 2000. Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface. Mol. Cell 5:629-638.
    • (2000) Mol. Cell , vol.5 , pp. 629-638
    • Leonhard, K.1    Guiard, B.2    Pellecchia, G.3    Tzagoloff, A.4    Neupert, W.5    Langer, T.6
  • 24
    • 0038394714 scopus 로고    scopus 로고
    • The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA-ATPase complexes to peroxisomes
    • Matsumoto, N., S. Tamura, and Y. Fujiki. 2003. The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA-ATPase complexes to peroxisomes. Nat. Cell Biol. 5:454-460.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 454-460
    • Matsumoto, N.1    Tamura, S.2    Fujiki, Y.3
  • 25
    • 0043167793 scopus 로고    scopus 로고
    • Mutations in novel peroxin gene PEX26 that cause peroxisome biogenesis disorders of complementation group 8 provide a genotype-phenotype correlation
    • Matsumoto, N., S. Tamura, S. Furuki, N. Miyata, A. Moser, N. Shimozawa, H. W. Moser, Y. Suzuki, N. Kondo, and Y. Fujiki. 2003. Mutations in novel peroxin gene PEX26 that cause peroxisome biogenesis disorders of complementation group 8 provide a genotype-phenotype correlation. Am. J. Hum. Genet. 73:233-246.
    • (2003) Am. J. Hum. Genet. , vol.73 , pp. 233-246
    • Matsumoto, N.1    Tamura, S.2    Furuki, S.3    Miyata, N.4    Moser, A.5    Shimozawa, N.6    Moser, H.W.7    Suzuki, Y.8    Kondo, N.9    Fujiki, Y.10
  • 27
    • 0026643496 scopus 로고
    • Carboxyl-terminal consensus Ser-Lys-Leu-related tripeptide of peroxisomal proteins functions in vitro as a minimal peroxisome-targeting signal
    • Miura, S., I. Kasuya-Arai, H. Mori, S. Miyazawa, T. Osumi, T. Hashimoto, and Y. Fujiki. 1992. Carboxyl-terminal consensus Ser-Lys-Leu-related tripeptide of peroxisomal proteins functions in vitro as a minimal peroxisome-targeting signal. J. Biol. Chem. 267:14405-14411.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14405-14411
    • Miura, S.1    Kasuya-Arai, I.2    Mori, H.3    Miyazawa, S.4    Osumi, T.5    Hashimoto, T.6    Fujiki, Y.7
  • 28
    • 0024528893 scopus 로고
    • Peroxisome targeting signal of rat liver acyl-coenzyme a oxidase resides at the carboxy terminus
    • Miyazawa, S., T. Osumi, T. Hashimoto, K. Ohno, S. Miura, and Y. Fujiki. 1989. Peroxisome targeting signal of rat liver acyl-coenzyme A oxidase resides at the carboxy terminus. Mol. Cell. Biol. 9:83-91.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 83-91
    • Miyazawa, S.1    Osumi, T.2    Hashimoto, T.3    Ohno, K.4    Miura, S.5    Fujiki, Y.6
  • 29
    • 0017237063 scopus 로고
    • Immunochemical and immuno-electron microscopic studies on localization of NADPH-cytochrome c reductase on rat liver microsomes
    • Morimoto, T., S. Matsuura, S. Sasaki, Y. Yashiro, and T. Omura. 1976. Immunochemical and immuno-electron microscopic studies on localization of NADPH-cytochrome c reductase on rat liver microsomes. J. Cell Biol. 68:189-201.
    • (1976) J. Cell Biol. , vol.68 , pp. 189-201
    • Morimoto, T.1    Matsuura, S.2    Sasaki, S.3    Yashiro, Y.4    Omura, T.5
  • 30
    • 0037088664 scopus 로고    scopus 로고
    • Intracellular localization, function, and dysfunction of the peroxisome-targeting signal type 2 receptor, Pex7p, in mammalian cells
    • Mukai, S., K. Ghaedi, and Y. Fujiki. 2002. Intracellular localization, function, and dysfunction of the peroxisome-targeting signal type 2 receptor, Pex7p, in mammalian cells. J. Biol. Chem. 277:9548-9561.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9548-9561
    • Mukai, S.1    Ghaedi, K.2    Fujiki, Y.3
  • 31
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert, W. 1997. Protein import into mitochondria. Annu. Rev. Biochem. 66:863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 32
    • 0034682844 scopus 로고    scopus 로고
    • Molecular anatomy of the peroxin Pex12p: RING finger domain is essential for the Pex12p function and interacts with the peroxisome targeting signal type 1-receptor Pex5p and a RING peroxin, Pex10p
    • Okumoto, K., I. Abe, and Y. Fujiki. 2000. Molecular anatomy of the peroxin Pex12p: RING finger domain is essential for the Pex12p function and interacts with the peroxisome targeting signal type 1-receptor Pex5p and a RING peroxin, Pex10p. J. Biol. Chem. 275:25700-25710.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25700-25710
    • Okumoto, K.1    Abe, I.2    Fujiki, Y.3
  • 33
    • 0031586033 scopus 로고    scopus 로고
    • Isolation and characterization of peroxisome-deficient Chinese hamster ovary cell mutants representing human complementation group III
    • Okumoto, K., A. Bogaki, K. Tateishi, T. Tsukamoto, T. Osumi, N. Shimozawa, Y. Suzuki, T. Orii, and Y. Fujiki. 1997. Isolation and characterization of peroxisome-deficient Chinese hamster ovary cell mutants representing human complementation group III. Exp. Cell Res. 233:11-20.
    • (1997) Exp. Cell Res. , vol.233 , pp. 11-20
    • Okumoto, K.1    Bogaki, A.2    Tateishi, K.3    Tsukamoto, T.4    Osumi, T.5    Shimozawa, N.6    Suzuki, Y.7    Orii, T.8    Fujiki, Y.9
  • 36
    • 0034647937 scopus 로고    scopus 로고
    • The mammalian peroxin Pex5pL, the longer isoform of mobile PTS1-transporter, translocates Pex7p-PTS2 protein complex into peroxisomes via its initial docking site Pex14p
    • Otera, H., T. Harano, M. Honsho, K. Ghaedi, S. Mukai, A. Tanaka, A. Kawai, N. Shimizu, and Y. Fujiki. 2000. The mammalian peroxin Pex5pL, the longer isoform of mobile PTS1-transporter, translocates Pex7p-PTS2 protein complex into peroxisomes via its initial docking site Pex14p. J. Biol. Chem. 275:21703-21714.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21703-21714
    • Otera, H.1    Harano, T.2    Honsho, M.3    Ghaedi, K.4    Mukai, S.5    Tanaka, A.6    Kawai, A.7    Shimizu, N.8    Fujiki, Y.9
  • 38
    • 0036179374 scopus 로고    scopus 로고
    • Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: Conserved Pex5p WXXXF/Y motifs are critical for matrix protein import
    • Otera, H., K. Setoguchi, M. Hamasaki, T. Kumashiro, N. Shimizu, and Y. Fujiki. 2002. Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import. Mol. Cell. Biol. 22:1639-1655.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1639-1655
    • Otera, H.1    Setoguchi, K.2    Hamasaki, M.3    Kumashiro, T.4    Shimizu, N.5    Fujiki, Y.6
  • 39
    • 23144446970 scopus 로고    scopus 로고
    • Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol
    • Platta, H. W., S. Grunau, K. Rosenkranz, W. Girzalsky, and R. Erdmann. 2005. Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol. Nat. Cell Biol. 7:817-822.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 817-822
    • Platta, H.W.1    Grunau, S.2    Rosenkranz, K.3    Girzalsky, W.4    Erdmann, R.5
  • 40
    • 0030720859 scopus 로고    scopus 로고
    • Human PEX1 is mutated in complementation group 1 of the peroxisome biogenesis disorders
    • Portsteffen, H., A. Beyer, E. Becker, C. Epplen, A. Pawlak, W.-H. Kunau, and G. Dodt. 1997. Human PEX1 is mutated in complementation group 1 of the peroxisome biogenesis disorders. Nat. Genet. 17:449-452.
    • (1997) Nat. Genet. , vol.17 , pp. 449-452
    • Portsteffen, H.1    Beyer, A.2    Becker, E.3    Epplen, C.4    Pawlak, A.5    Kunau, W.-H.6    Dodt, G.7
  • 41
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport, T. A., B. Jungnickel, and U. Kutay. 1996. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65:271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 43
    • 0034515057 scopus 로고    scopus 로고
    • The genetics of peroxisome biogenesis
    • Sacksteder, K. A., and S. J. Gould. 2000. The genetics of peroxisome biogenesis. Annu. Rev. Genet. 34:623-652.
    • (2000) Annu. Rev. Genet. , vol.34 , pp. 623-652
    • Sacksteder, K.A.1    Gould, S.J.2
  • 44
    • 0033617195 scopus 로고    scopus 로고
    • The peroxin Pex14p: CDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis
    • Shimizu, N., R. Itoh, Y. Hirono, H. Otera, K. Ghaedi, K. Tateishi, S. Tamura, K. Okumoto, T. Harano, S. Mukai, and Y. Fujiki. 1999. The peroxin Pex14p: cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis. J. Biol. Chem. 274:12593-12604.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12593-12604
    • Shimizu, N.1    Itoh, R.2    Hirono, Y.3    Otera, H.4    Ghaedi, K.5    Tateishi, K.6    Tamura, S.7    Okumoto, K.8    Harano, T.9    Mukai, S.10    Fujiki, Y.11
  • 45
    • 0033787313 scopus 로고    scopus 로고
    • Import of peroxisomal matrix and membrane proteins
    • Subramani, S., A. Koller, and W. B. Snyder. 2000. Import of peroxisomal matrix and membrane proteins. Annu. Rev. Biochem. 69:399-418.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 399-418
    • Subramani, S.1    Koller, A.2    Snyder, W.B.3
  • 46
    • 0035878969 scopus 로고    scopus 로고
    • Phenotype-genotype relationships in peroxisome biogenesis disorders of PEX1-defective complementation group 1 are defined by Pex1p-Pex6p interaction
    • Tamura, S., N. Matsumoto, A. Imamura, N. Shimozawa, Y. Suzuki, N. Kondo, and Y. Fujiki. 2001. Phenotype-genotype relationships in peroxisome biogenesis disorders of PEX1-defective complementation group 1 are defined by Pex1p-Pex6p interaction. Biochem. J. 357:417-426.
    • (2001) Biochem. J. , vol.357 , pp. 417-426
    • Tamura, S.1    Matsumoto, N.2    Imamura, A.3    Shimozawa, N.4    Suzuki, Y.5    Kondo, N.6    Fujiki, Y.7
  • 47
    • 0032515992 scopus 로고    scopus 로고
    • Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group I
    • Tamura, S., K. Okumoto, R. Toyama, N. Shimozawa, T. Tsukamoto, Y. Suzuki, T. Osumi, N. Kondo, and Y. Fujiki. 1998. Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group I. Proc. Natl. Acad. Sci. USA 95:4350-4355.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4350-4355
    • Tamura, S.1    Okumoto, K.2    Toyama, R.3    Shimozawa, N.4    Tsukamoto, T.5    Suzuki, Y.6    Osumi, T.7    Kondo, N.8    Fujiki, Y.9
  • 49
    • 0029087571 scopus 로고
    • The Pichia pastoris peroxisomal protein PAS8p is the receptor for the C-terminal tripeptide peroxisome targeting signal
    • Terlecky, S. R., W. M. Nuttley, D. McCollum, E. Sock, and S. Subramani. 1995. The Pichia pastoris peroxisomal protein PAS8p is the receptor for the C-terminal tripeptide peroxisome targeting signal. EMBO J. 14:3627-3634.
    • (1995) EMBO J. , vol.14 , pp. 3627-3634
    • Terlecky, S.R.1    Nuttley, W.M.2    McCollum, D.3    Sock, E.4    Subramani, S.5
  • 51
    • 0026064431 scopus 로고
    • Restoration by a 35K membrane protein of peroxisome assembly in a peroxisome-deficient mammalian cell mutant
    • Tsukamoto, T., S. Miura, and Y. Fujiki. 1991. Restoration by a 35K membrane protein of peroxisome assembly in a peroxisome-deficient mammalian cell mutant. Nature 350:77-81.
    • (1991) Nature , vol.350 , pp. 77-81
    • Tsukamoto, T.1    Miura, S.2    Fujiki, Y.3
  • 53
    • 0025342563 scopus 로고
    • Isolation and characterization of Chinese hamster ovary cell mutants defective in assembly of peroxisomes
    • Tsukamoto, T., S. Yokota, and Y. Fujiki. 1990. Isolation and characterization of Chinese hamster ovary cell mutants defective in assembly of peroxisomes. J. Cell Biol. 110:651-660.
    • (1990) J. Cell Biol. , vol.110 , pp. 651-660
    • Tsukamoto, T.1    Yokota, S.2    Fujiki, Y.3
  • 55
    • 0027138676 scopus 로고
    • PAS10 is a tetratricopeptide-repeat protein that is essential for the import of most matrix proteins into peroxisomes of Saccharomyces cerevisiae
    • Van der Leij, I., M. M. Franse, Y. Elgersma, B. Distel, and H. F. Tabak. 1993. PAS10 is a tetratricopeptide-repeat protein that is essential for the import of most matrix proteins into peroxisomes of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 90:11782-11786.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11782-11786
    • Van Der Leij, I.1    Franse, M.M.2    Elgersma, Y.3    Distel, B.4    Tabak, H.F.5
  • 57
    • 0029888487 scopus 로고    scopus 로고
    • The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a cytoplasmic ATPase required for stability of the PTS1 receptor
    • Yahraus, T., N. Braverman, G. Dodt, J. E. Kalish, J. C. Morrell, H. W. Moser, D. Valle, and S. J. Gould. 1996. The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a cytoplasmic ATPase required for stability of the PTS1 receptor. EMBO J. 15:2914-2923.
    • (1996) EMBO J. , vol.15 , pp. 2914-2923
    • Yahraus, T.1    Braverman, N.2    Dodt, G.3    Kalish, J.E.4    Morrell, J.C.5    Moser, H.W.6    Valle, D.7    Gould, S.J.8
  • 58
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., H. H. Meyer, and T. A. Rapoport. 2001. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414:652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.